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Published October 1995 | public
Journal Article

Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface

Abstract

Phosphotransfer between the autophosphorylating histidine kinase CheA and the response regulator CheY represents a crucial step in the bacterial chemotaxis signal transduction pathway. The ^(15)N−^1H correlation spectrum of CheY complexed with an amino-terminal fragment of CheA exhibits specific localized differences in chemical shifts when compared to the spectrum of uncompiexed CheY. When mapped onto the three-dimensional structure of CheY, these changes define a region distinct from the active site. A single amino-acid substitution within this binding region on CheY, alanine to valine at position 103, significantly decreases the affinity of CheY for CheA. The binding face described by these changes partially overlaps a flagellar switch binding surface previously defined by mutagenesis.

Additional Information

© 1995 Nature Publishing Group. Received 7 July; Accepted 7 August 1995. Supported by U S. Public Health Service Grants (M.I.S), (F.W.D), (P.M.), Cancer Research Fund of the Damon Runyon-Walter Winchell Foundation Fellowship (D.F.L.), National Research Service Award Fellowship (R.V.S.), and a National Research Service Award Pre-doctoral Training Grant from NIH (M.M.M).

Additional details

Created:
August 20, 2023
Modified:
October 23, 2023